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Database: PDB
Entry: 2OXE
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HEADER    HYDROLASE                               20-FEB-07   2OXE              
TITLE     STRUCTURE OF THE HUMAN PANCREATIC LIPASE-RELATED PROTEIN 2            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PANCREATIC LIPASE-RELATED PROTEIN 2;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: PANCREAS;                                                    
SOURCE   6 GENE: PNLIPRP2, PLRP2;                                               
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: HIGH5;                                     
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PAB-BEE                                   
KEYWDS    GLYCOPROTEIN, HYDROLASE, LIPID DEGRADATION, PANCREATIC LIPASE,        
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WALKER,T.DAVIS,A.SEITOVA,P.J.FINERTY JR.,C.BUTLER-COLE,           
AUTHOR   2 I.KOZIERADZKI,J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,      
AUTHOR   3 A.BOCHKAREV,S.DHE-PAGANON,STRUCTURAL GENOMICS CONSORTIUM (SGC)       
REVDAT   5   13-JUL-11 2OXE    1       VERSN                                    
REVDAT   4   09-JUN-09 2OXE    1       REVDAT                                   
REVDAT   3   24-FEB-09 2OXE    1       VERSN                                    
REVDAT   2   20-JAN-09 2OXE    1       JRNL                                     
REVDAT   1   27-MAR-07 2OXE    0                                                
JRNL        AUTH   C.EYDOUX,S.SPINELLI,T.L.DAVIS,J.R.WALKER,A.SEITOVA,          
JRNL        AUTH 2 S.DHE-PAGANON,A.DE CARO,C.CAMBILLAU,F.CARRIERE               
JRNL        TITL   STRUCTURE OF HUMAN PANCREATIC LIPASE-RELATED PROTEIN 2 WITH  
JRNL        TITL 2 THE LID IN AN OPEN CONFORMATION.                             
JRNL        REF    BIOCHEMISTRY                  V.  47  9553 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18702514                                                     
JRNL        DOI    10.1021/BI8005576                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.SIAS,F.FERRATO,P.GRANDVAL,D.LAFONT,P.BOULLANGER,A.DE CARO, 
REMARK   1  AUTH 2 B.LEBOEUF,R.VERGER,F.CARRIERE                                
REMARK   1  TITL   HUMAN PANCREATIC LIPASE-RELATED PROTEIN 2 IS A GALACTOLIPASE 
REMARK   1  REF    BIOCHEMISTRY                  V.  43 10138 2004              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   15287741                                                     
REMARK   1  DOI    10.1021/BI049818D                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.GILLER,P.BUCHWALD,D.BLUM-KAELIN,W.HUNZIKER                 
REMARK   1  TITL   TWO NOVEL HUMAN PANCREATIC LIPASE RELATED PROTEINS, HPLRP1   
REMARK   1  TITL 2 AND HPLRP2                                                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 267 16509 1992              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   1379598                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 34305                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1811                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2464                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 122                          
REMARK   3   BIN FREE R VALUE                    : 0.4430                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6642                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 129                                     
REMARK   3   SOLVENT ATOMS            : 76                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.11000                                              
REMARK   3    B22 (A**2) : 4.11000                                              
REMARK   3    B33 (A**2) : -8.22000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.641         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.334         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.314         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.297        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6997 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9525 ; 1.142 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   868 ; 5.275 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   327 ;36.635 ;24.587       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1045 ;17.520 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;16.800 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1034 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5401 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3124 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4783 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   221 ; 0.133 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     5 ; 0.092 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    49 ; 0.169 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.079 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4404 ; 0.322 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6915 ; 0.585 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2925 ; 0.885 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2610 ; 1.650 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    18        A    63                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7530 -16.2590  50.2980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2429 T22:   0.1912                                     
REMARK   3      T33:   0.1878 T12:   0.0457                                     
REMARK   3      T13:   0.0187 T23:   0.0940                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0568 L22:   2.5774                                     
REMARK   3      L33:   1.6249 L12:  -0.8243                                     
REMARK   3      L13:  -0.1866 L23:  -0.3465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2684 S12:  -0.1971 S13:  -0.0033                       
REMARK   3      S21:  -0.1005 S22:  -0.1928 S23:   0.1199                       
REMARK   3      S31:   0.3780 S32:  -0.0100 S33:  -0.0756                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    64        A    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.7160 -24.9230  50.3660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3034 T22:   0.2636                                     
REMARK   3      T33:   0.3846 T12:   0.4909                                     
REMARK   3      T13:   0.0950 T23:   0.1230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7909 L22:   3.2326                                     
REMARK   3      L33:  11.7935 L12:   2.3833                                     
REMARK   3      L13:   1.9150 L23:   4.1921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3900 S12:  -0.5980 S13:  -0.6397                       
REMARK   3      S21:   0.0637 S22:  -0.0280 S23:  -0.7258                       
REMARK   3      S31:   1.2455 S32:   0.9978 S33:  -0.3620                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    87        A   172                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6680 -14.5190  46.1740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1883 T22:   0.2839                                     
REMARK   3      T33:   0.2986 T12:   0.1894                                     
REMARK   3      T13:   0.1257 T23:   0.1297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2570 L22:   1.6108                                     
REMARK   3      L33:   1.7370 L12:  -0.4256                                     
REMARK   3      L13:   0.3245 L23:   0.5498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0913 S12:   0.0174 S13:  -0.0524                       
REMARK   3      S21:  -0.2257 S22:  -0.0428 S23:  -0.2688                       
REMARK   3      S31:   0.5214 S32:   0.3487 S33:   0.1341                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   173        A   212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5470  -3.9890  51.0930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1017 T22:   0.2547                                     
REMARK   3      T33:   0.3789 T12:   0.0609                                     
REMARK   3      T13:   0.0883 T23:   0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9233 L22:   1.8564                                     
REMARK   3      L33:   3.5426 L12:   0.8157                                     
REMARK   3      L13:   0.3579 L23:   0.1873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0643 S12:   0.0856 S13:  -0.1640                       
REMARK   3      S21:  -0.1610 S22:   0.0857 S23:   0.0301                       
REMARK   3      S31:  -0.1614 S32:   0.1224 S33:  -0.1500                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   213        A   249                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4270   3.8490  43.1950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1066 T22:   0.2249                                     
REMARK   3      T33:   0.4574 T12:   0.0451                                     
REMARK   3      T13:   0.1645 T23:   0.0544                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5520 L22:   3.5500                                     
REMARK   3      L33:   4.5152 L12:   1.2982                                     
REMARK   3      L13:  -2.2151 L23:  -0.0265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0184 S12:  -0.2368 S13:   0.5269                       
REMARK   3      S21:   0.0040 S22:  -0.0143 S23:   0.4057                       
REMARK   3      S31:  -0.5860 S32:  -0.3264 S33:  -0.0041                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   250        A   303                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3920   0.2430  34.3590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0984 T22:   0.2325                                     
REMARK   3      T33:   0.4182 T12:   0.1041                                     
REMARK   3      T13:   0.1818 T23:   0.0894                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6109 L22:   3.3725                                     
REMARK   3      L33:   5.1912 L12:   0.7994                                     
REMARK   3      L13:  -1.1489 L23:   0.2070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2572 S12:   0.4392 S13:   0.3579                       
REMARK   3      S21:  -0.5727 S22:  -0.2579 S23:  -0.0339                       
REMARK   3      S31:  -0.0498 S32:   0.2211 S33:   0.0007                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   304        A   327                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8530  15.4710  40.1130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0710 T22:   0.1798                                     
REMARK   3      T33:   0.5069 T12:  -0.0720                                     
REMARK   3      T13:   0.3634 T23:  -0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0225 L22:   9.2111                                     
REMARK   3      L33:   9.5232 L12:   2.8303                                     
REMARK   3      L13:  -0.0553 L23:  -2.3876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2384 S12:  -0.4434 S13:   0.9962                       
REMARK   3      S21:  -0.1740 S22:  -0.0351 S23:  -0.2819                       
REMARK   3      S31:  -1.2440 S32:   0.1058 S33:  -0.2033                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   328        A   366                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.7700   9.8220  38.6010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0700 T22:   0.2713                                     
REMARK   3      T33:   0.5476 T12:  -0.0065                                     
REMARK   3      T13:   0.2429 T23:   0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8658 L22:   1.9236                                     
REMARK   3      L33:   2.9555 L12:   2.2704                                     
REMARK   3      L13:  -2.3864 L23:  -2.2384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3708 S12:  -0.3301 S13:   0.5511                       
REMARK   3      S21:   0.0438 S22:  -0.1710 S23:  -0.3255                       
REMARK   3      S31:  -0.3630 S32:   0.4278 S33:  -0.1998                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   367        A   397                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.4650  21.4890  19.1820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0700 T22:   0.1127                                     
REMARK   3      T33:   0.3777 T12:  -0.0601                                     
REMARK   3      T13:   0.3543 T23:   0.1395                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.1182 L22:  14.9009                                     
REMARK   3      L33:   5.7730 L12:  -2.2561                                     
REMARK   3      L13:  -3.4704 L23:   2.3067                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2446 S12:   0.9448 S13:   0.9263                       
REMARK   3      S21:  -0.4840 S22:   0.3499 S23:   0.6312                       
REMARK   3      S31:  -0.7164 S32:  -0.3641 S33:  -0.5945                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   398        A   469                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.6810  22.6790  23.4510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0406 T22:   0.0793                                     
REMARK   3      T33:   0.5736 T12:  -0.0550                                     
REMARK   3      T13:   0.3078 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0639 L22:   5.8218                                     
REMARK   3      L33:   6.2832 L12:   3.1134                                     
REMARK   3      L13:  -4.3864 L23:  -4.2600                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3189 S12:  -0.0577 S13:   1.0425                       
REMARK   3      S21:  -0.1904 S22:   0.3565 S23:   0.1671                       
REMARK   3      S31:  -0.3056 S32:  -0.2934 S33:  -0.6755                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    18        B    63                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9730  13.4290  13.0120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3385 T22:   0.2605                                     
REMARK   3      T33:   0.0586 T12:   0.1210                                     
REMARK   3      T13:  -0.1972 T23:  -0.0710                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7150 L22:   7.0938                                     
REMARK   3      L33:   1.4876 L12:   0.1148                                     
REMARK   3      L13:   0.0131 L23:   0.3334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1965 S12:   0.2529 S13:  -0.1019                       
REMARK   3      S21:  -0.6480 S22:   0.0634 S23:   0.1155                       
REMARK   3      S31:  -0.2393 S32:  -0.6411 S33:   0.1331                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    64        B    86                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.5600  35.1530  11.9290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3849 T22:   0.2733                                     
REMARK   3      T33:   0.5461 T12:   0.3700                                     
REMARK   3      T13:  -0.3599 T23:   0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1223 L22:   8.7586                                     
REMARK   3      L33:  14.1609 L12:   4.2343                                     
REMARK   3      L13:  -8.4860 L23:  -8.6073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5574 S12:   1.1703 S13:   1.3852                       
REMARK   3      S21:  -0.7267 S22:   0.9758 S23:   0.8889                       
REMARK   3      S31:  -1.1151 S32:  -1.8979 S33:  -0.4183                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    87        B   172                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.6680  25.6570  17.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3608 T22:   0.1744                                     
REMARK   3      T33:   0.2250 T12:   0.1913                                     
REMARK   3      T13:  -0.1596 T23:  -0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9955 L22:   2.0983                                     
REMARK   3      L33:   2.4803 L12:   0.9991                                     
REMARK   3      L13:   0.4596 L23:   1.4147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2056 S12:   0.1623 S13:   0.1988                       
REMARK   3      S21:  -0.0950 S22:   0.0323 S23:   0.2632                       
REMARK   3      S31:  -0.4762 S32:  -0.5247 S33:   0.1732                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   173        B   212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7730  17.1870  12.8260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3142 T22:   0.1427                                     
REMARK   3      T33:   0.2357 T12:  -0.0019                                     
REMARK   3      T13:  -0.0570 T23:  -0.0945                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3852 L22:   7.0607                                     
REMARK   3      L33:   6.6380 L12:   0.4162                                     
REMARK   3      L13:  -0.0940 L23:   0.4298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0472 S12:   0.2286 S13:  -0.1347                       
REMARK   3      S21:  -0.5216 S22:   0.0490 S23:   0.0453                       
REMARK   3      S31:  -0.0287 S32:   0.1465 S33:  -0.0018                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   213        B   253                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8860  18.2050  22.3160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2569 T22:   0.1360                                     
REMARK   3      T33:   0.3136 T12:   0.0290                                     
REMARK   3      T13:  -0.0299 T23:  -0.0728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1737 L22:   3.9393                                     
REMARK   3      L33:   2.5598 L12:   1.5172                                     
REMARK   3      L13:  -1.1704 L23:   0.2565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2529 S12:   0.0487 S13:  -0.3415                       
REMARK   3      S21:  -0.1693 S22:   0.1054 S23:  -0.5748                       
REMARK   3      S31:  -0.1881 S32:   0.1506 S33:   0.1475                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   254        B   303                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1660  26.6470  29.4570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4201 T22:   0.1585                                     
REMARK   3      T33:   0.3323 T12:   0.0482                                     
REMARK   3      T13:  -0.0866 T23:  -0.0742                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4462 L22:   1.4102                                     
REMARK   3      L33:   1.0418 L12:   0.3687                                     
REMARK   3      L13:  -0.6177 L23:  -0.0559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1273 S12:  -0.4184 S13:   0.1878                       
REMARK   3      S21:   0.2200 S22:  -0.0994 S23:   0.2720                       
REMARK   3      S31:  -0.4351 S32:  -0.1240 S33:  -0.0279                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   304        B   327                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7650  28.0710  24.9540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3849 T22:   0.0869                                     
REMARK   3      T33:   0.4115 T12:  -0.2010                                     
REMARK   3      T13:   0.0151 T23:  -0.1562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8774 L22:   1.6739                                     
REMARK   3      L33:   8.4874 L12:   0.6451                                     
REMARK   3      L13:   2.0778 L23:  -3.4571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3165 S12:   0.4260 S13:   0.0903                       
REMARK   3      S21:  -0.4771 S22:  -0.1875 S23:  -0.9723                       
REMARK   3      S31:  -0.4195 S32:   1.2771 S33:   0.5041                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   328        B   366                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1550  31.8010  26.2020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4590 T22:   0.0047                                     
REMARK   3      T33:   0.3253 T12:  -0.0748                                     
REMARK   3      T13:   0.0145 T23:  -0.0858                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0257 L22:   1.6328                                     
REMARK   3      L33:   3.1353 L12:   1.6757                                     
REMARK   3      L13:   2.1666 L23:   2.2564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2105 S12:   0.2475 S13:   0.2822                       
REMARK   3      S21:  -0.3497 S22:   0.3449 S23:  -0.3200                       
REMARK   3      S31:  -0.4595 S32:   0.5299 S33:  -0.1344                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   367        B   398                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.9870  36.6540  46.4890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1839 T22:  -0.0678                                     
REMARK   3      T33:   0.4383 T12:  -0.0190                                     
REMARK   3      T13:  -0.0458 T23:  -0.1598                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9036 L22:   7.1360                                     
REMARK   3      L33:  11.2234 L12:  -2.3686                                     
REMARK   3      L13:   3.1522 L23:   0.8050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:  -1.2230 S13:  -0.1091                       
REMARK   3      S21:   0.7916 S22:   0.2052 S23:  -0.1562                       
REMARK   3      S31:   0.7032 S32:  -0.4561 S33:  -0.2553                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   399        B   469                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5070  41.6460  41.9600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1273 T22:   0.0535                                     
REMARK   3      T33:   0.4489 T12:  -0.0421                                     
REMARK   3      T13:   0.0042 T23:  -0.2369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8107 L22:   3.3079                                     
REMARK   3      L33:   5.6235 L12:   0.7766                                     
REMARK   3      L13:   3.2048 L23:   3.8097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2419 S12:  -0.2859 S13:   0.2090                       
REMARK   3      S21:  -0.1154 S22:   0.4869 S23:  -0.4107                       
REMARK   3      S31:   0.1214 S32:   0.2969 S33:  -0.2450                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B           
REMARK   3  FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS   
REMARK   4                                                                      
REMARK   4 2OXE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041703.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36137                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.78500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.760                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BU8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.17M AMMONIUM SULFATE, 0.1M SODIUM      
REMARK 280  CACODYLATE PH 5.5, 0.04M NACL, CRYOPROTECTED WITH 15% GLYCEROL,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, PH 5.50            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000      108.46100            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.80900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.90450            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      108.46100            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       92.71350            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       92.71350            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      108.46100            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       30.90450            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000      108.46100            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.80900            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000      108.46100            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       61.80900            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000      108.46100            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       92.71350            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       30.90450            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      108.46100            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       30.90450            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       92.71350            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000      108.46100            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000      108.46100            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       61.80900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     LYS A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     ASN A   259                                                      
REMARK 465     VAL A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     SER A   262                                                      
REMARK 465     THR A   263                                                      
REMARK 465     ILE A   264                                                      
REMARK 465     THR A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     ILE A   267                                                      
REMARK 465     ARG A   425                                                      
REMARK 465     GLY A   426                                                      
REMARK 465     ILE A   427                                                      
REMARK 465     ASN A   428                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     SER A   430                                                      
REMARK 465     GLU A   470                                                      
REMARK 465     PHE A   471                                                      
REMARK 465     VAL A   472                                                      
REMARK 465     GLU A   473                                                      
REMARK 465     HIS A   474                                                      
REMARK 465     HIS A   475                                                      
REMARK 465     HIS A   476                                                      
REMARK 465     HIS A   477                                                      
REMARK 465     HIS A   478                                                      
REMARK 465     HIS A   479                                                      
REMARK 465     HIS A   480                                                      
REMARK 465     HIS A   481                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     LYS B   258                                                      
REMARK 465     ASN B   259                                                      
REMARK 465     VAL B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     SER B   262                                                      
REMARK 465     THR B   263                                                      
REMARK 465     ILE B   264                                                      
REMARK 465     THR B   265                                                      
REMARK 465     ASP B   266                                                      
REMARK 465     ILE B   267                                                      
REMARK 465     ASP B   268                                                      
REMARK 465     GLY B   269                                                      
REMARK 465     ILE B   270                                                      
REMARK 465     TRP B   271                                                      
REMARK 465     GLU B   272                                                      
REMARK 465     ARG B   425                                                      
REMARK 465     GLY B   426                                                      
REMARK 465     ILE B   427                                                      
REMARK 465     ASN B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     GLU B   470                                                      
REMARK 465     PHE B   471                                                      
REMARK 465     VAL B   472                                                      
REMARK 465     GLU B   473                                                      
REMARK 465     HIS B   474                                                      
REMARK 465     HIS B   475                                                      
REMARK 465     HIS B   476                                                      
REMARK 465     HIS B   477                                                      
REMARK 465     HIS B   478                                                      
REMARK 465     HIS B   479                                                      
REMARK 465     HIS B   480                                                      
REMARK 465     HIS B   481                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  18    CG   CD   CE   NZ                                   
REMARK 470     LYS A 251    CD   CE   NZ                                        
REMARK 470     ILE A 274    O                                                   
REMARK 470     LYS A 314    CG   CD   CE   NZ                                   
REMARK 470     GLU A 321    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 334    CD   CE   NZ                                        
REMARK 470     LYS A 368    CG   CD   CE   NZ                                   
REMARK 470     GLU A 369    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 370    CB   CG   CD   CE   NZ                              
REMARK 470     ARG A 376    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 384    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 393    CG   CD   CE   NZ                                   
REMARK 470     LYS A 397    CG   CD   CE   NZ                                   
REMARK 470     LYS A 417    CG   CD   CE   NZ                                   
REMARK 470     LYS A 424    CG   CD   CE   NZ                                   
REMARK 470     GLU A 459    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B  18    CG   CD   CE   NZ                                   
REMARK 470     GLU B  31    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  88    CD   CE   NZ                                        
REMARK 470     LYS B 117    CG   CD   CE   NZ                                   
REMARK 470     LEU B 158    CG   CD1  CD2                                       
REMARK 470     GLU B 321    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 334    CG   CD   CE   NZ                                   
REMARK 470     LYS B 368    CG   CD   CE   NZ                                   
REMARK 470     LYS B 370    CB   CG   CD   CE   NZ                              
REMARK 470     GLU B 384    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 393    CE   NZ                                             
REMARK 470     LYS B 397    CG   CD   CE   NZ                                   
REMARK 470     LYS B 424    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 102       50.24     38.44                                   
REMARK 500    SER A 171     -119.04     60.27                                   
REMARK 500    ASP A 195       65.98     38.07                                   
REMARK 500    CYS A 200       17.69     83.82                                   
REMARK 500    PHE A 201      -44.75   -140.62                                   
REMARK 500    CYS A 315       54.08   -112.92                                   
REMARK 500    PRO A 317     -161.53    -79.68                                   
REMARK 500    PHE A 354       -2.83     66.95                                   
REMARK 500    GLU A 384     -161.08   -160.70                                   
REMARK 500    ASP A 399      -12.61     76.98                                   
REMARK 500    SER A 454      139.44   -174.90                                   
REMARK 500    GLU A 460      136.42    -33.63                                   
REMARK 500    ASN A 461       -9.35     73.58                                   
REMARK 500    SER B  81     -167.52   -104.24                                   
REMARK 500    SER B 171     -108.63     43.78                                   
REMARK 500    ASP B 195       67.28     35.97                                   
REMARK 500    CYS B 200       -4.36     82.25                                   
REMARK 500    ASP B 203       -5.44     71.35                                   
REMARK 500    PRO B 317     -160.01    -75.22                                   
REMARK 500    ASN B 383      -50.59   -133.48                                   
REMARK 500    LEU B 396       60.71   -107.85                                   
REMARK 500    ASP B 399      -11.55     81.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 214   OD1                                                    
REMARK 620 2 ARG A 209   O   129.1                                              
REMARK 620 3 GLU A 206   O   147.3  80.6                                        
REMARK 620 4 ASP A 214   OD2  47.9  82.1 149.6                                  
REMARK 620 5 HOH A 617   O    96.2  82.1 102.1 100.1                            
REMARK 620 6 ASP A 211   OD2  86.3  89.8  79.7  75.4 171.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG B 209   O                                                      
REMARK 620 2 ASP B 211   OD2  99.5                                              
REMARK 620 3 ASP B 214   OD1 125.9  74.3                                        
REMARK 620 4 ASP B 214   OD2  79.7  69.6  47.2                                  
REMARK 620 5 GLU B 206   O    84.5  78.4 141.8 141.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 5                    
DBREF  2OXE A   18   469  UNP    P54317   LIPR2_HUMAN     18    469             
DBREF  2OXE B   18   469  UNP    P54317   LIPR2_HUMAN     18    469             
SEQADV 2OXE ALA A   16  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE ALA A   17  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE GLU A  470  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE PHE A  471  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE VAL A  472  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE GLU A  473  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  474  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  475  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  476  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  477  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  478  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  479  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  480  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS A  481  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE ALA B   16  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE ALA B   17  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE GLU B  470  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE PHE B  471  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE VAL B  472  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE GLU B  473  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  474  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  475  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  476  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  477  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  478  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  479  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  480  UNP  P54317              CLONING ARTIFACT               
SEQADV 2OXE HIS B  481  UNP  P54317              CLONING ARTIFACT               
SEQRES   1 A  466  ALA ALA LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE          
SEQRES   2 A  466  SER ASP GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO          
SEQRES   3 A  466  VAL LYS LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR          
SEQRES   4 A  466  ARG PHE LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE          
SEQRES   5 A  466  GLN LEU ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA          
SEQRES   6 A  466  SER ASN PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE          
SEQRES   7 A  466  HIS GLY PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER          
SEQRES   8 A  466  ASP MET CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN          
SEQRES   9 A  466  CYS ILE CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET          
SEQRES  10 A  466  TYR THR GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA          
SEQRES  11 A  466  GLU THR ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU          
SEQRES  12 A  466  GLY TYR SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER          
SEQRES  13 A  466  LEU GLY ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU          
SEQRES  14 A  466  GLY GLY ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA          
SEQRES  15 A  466  GLY PRO CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU          
SEQRES  16 A  466  ASP PRO SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR          
SEQRES  17 A  466  ASP SER SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET          
SEQRES  18 A  466  SER GLN LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY          
SEQRES  19 A  466  GLY LYS GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER          
SEQRES  20 A  466  THR ILE THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY          
SEQRES  21 A  466  GLY PHE VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR          
SEQRES  22 A  466  TYR SER SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY          
SEQRES  23 A  466  TYR PRO CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS          
SEQRES  24 A  466  CYS PHE PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY          
SEQRES  25 A  466  HIS TYR ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL          
SEQRES  26 A  466  GLU GLN THR PHE PHE LEU ASN THR GLY GLU SER GLY ASN          
SEQRES  27 A  466  PHE THR SER TRP ARG TYR LYS VAL SER VAL THR LEU SER          
SEQRES  28 A  466  GLY LYS GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU          
SEQRES  29 A  466  TYR GLY SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE          
SEQRES  30 A  466  LYS GLY SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA          
SEQRES  31 A  466  ILE ASP VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL          
SEQRES  32 A  466  LYS PHE LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU          
SEQRES  33 A  466  PRO LYS LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY          
SEQRES  34 A  466  GLU ASP GLY THR GLU TYR ASN PHE CYS SER SER ASP THR          
SEQRES  35 A  466  VAL GLU GLU ASN VAL LEU GLN SER LEU TYR PRO CYS GLU          
SEQRES  36 A  466  PHE VAL GLU HIS HIS HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  466  ALA ALA LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE          
SEQRES   2 B  466  SER ASP GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO          
SEQRES   3 B  466  VAL LYS LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR          
SEQRES   4 B  466  ARG PHE LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE          
SEQRES   5 B  466  GLN LEU ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA          
SEQRES   6 B  466  SER ASN PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE          
SEQRES   7 B  466  HIS GLY PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER          
SEQRES   8 B  466  ASP MET CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN          
SEQRES   9 B  466  CYS ILE CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET          
SEQRES  10 B  466  TYR THR GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA          
SEQRES  11 B  466  GLU THR ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU          
SEQRES  12 B  466  GLY TYR SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER          
SEQRES  13 B  466  LEU GLY ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU          
SEQRES  14 B  466  GLY GLY ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA          
SEQRES  15 B  466  GLY PRO CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU          
SEQRES  16 B  466  ASP PRO SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR          
SEQRES  17 B  466  ASP SER SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET          
SEQRES  18 B  466  SER GLN LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY          
SEQRES  19 B  466  GLY LYS GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER          
SEQRES  20 B  466  THR ILE THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY          
SEQRES  21 B  466  GLY PHE VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR          
SEQRES  22 B  466  TYR SER SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY          
SEQRES  23 B  466  TYR PRO CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS          
SEQRES  24 B  466  CYS PHE PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY          
SEQRES  25 B  466  HIS TYR ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL          
SEQRES  26 B  466  GLU GLN THR PHE PHE LEU ASN THR GLY GLU SER GLY ASN          
SEQRES  27 B  466  PHE THR SER TRP ARG TYR LYS VAL SER VAL THR LEU SER          
SEQRES  28 B  466  GLY LYS GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU          
SEQRES  29 B  466  TYR GLY SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE          
SEQRES  30 B  466  LYS GLY SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA          
SEQRES  31 B  466  ILE ASP VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL          
SEQRES  32 B  466  LYS PHE LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU          
SEQRES  33 B  466  PRO LYS LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY          
SEQRES  34 B  466  GLU ASP GLY THR GLU TYR ASN PHE CYS SER SER ASP THR          
SEQRES  35 B  466  VAL GLU GLU ASN VAL LEU GLN SER LEU TYR PRO CYS GLU          
SEQRES  36 B  466  PHE VAL GLU HIS HIS HIS HIS HIS HIS HIS HIS                  
MODRES 2OXE ASN A  353  ASN  GLYCOSYLATION SITE                                 
MODRES 2OXE ASN B  353  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 500      14                                                       
HET    NAG  A 501      14                                                       
HET    MAN  A 502      11                                                       
HET    MAN  A 503      11                                                       
HET    MAN  A 504      11                                                       
HET    NAG  B 500      14                                                       
HET    NAG  B 501      14                                                       
HET    MAN  B 502      11                                                       
HET    MAN  B 503      11                                                       
HET    MAN  B 504      11                                                       
HET     CA  A 600       1                                                       
HET     CA  B 600       1                                                       
HET     CL  A   1       1                                                       
HET     CL  B   2       1                                                       
HET     CL  A   3       1                                                       
HET     CL  B   4       1                                                       
HET     CL  B   5       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   3  MAN    6(C6 H12 O6)                                                 
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   7   CL    5(CL 1-)                                                     
FORMUL  12  HOH   *76(H2 O)                                                     
HELIX    1   1 GLY A   23  LEU A   25  5                                   3    
HELIX    2   2 SER A   48  ASP A   53  1                                   6    
HELIX    3   3 PRO A   75  SER A   81  1                                   7    
HELIX    4   4 SER A  103  PHE A  113  1                                  11    
HELIX    5   5 TRP A  125  ARG A  130  1                                   6    
HELIX    6   6 MET A  132  GLY A  159  1                                  28    
HELIX    7   7 SER A  161  GLU A  163  5                                   3    
HELIX    8   8 LEU A  172  LEU A  184  1                                  13    
HELIX    9   9 ASP A  211  ALA A  215  5                                   5    
HELIX   10  10 GLY A  275  VAL A  278  5                                   4    
HELIX   11  11 SER A  279  ASN A  295  1                                  17    
HELIX   12  12 SER A  306  GLU A  312  1                                   7    
HELIX   13  13 TYR A  329  PHE A  333  5                                   5    
HELIX   14  14 GLY B   23  LEU B   25  5                                   3    
HELIX   15  15 SER B   48  ASP B   53  1                                   6    
HELIX   16  16 PRO B   75  ALA B   80  1                                   6    
HELIX   17  17 SER B  103  GLU B  116  1                                  14    
HELIX   18  18 TRP B  125  ARG B  130  1                                   6    
HELIX   19  19 TYR B  133  GLY B  159  1                                  27    
HELIX   20  20 SER B  161  GLU B  163  5                                   3    
HELIX   21  21 SER B  171  LEU B  184  1                                  14    
HELIX   22  22 ASP B  211  ALA B  215  5                                   5    
HELIX   23  23 GLY B  275  SER B  279  5                                   5    
HELIX   24  24 SER B  285  ASN B  295  1                                  11    
HELIX   25  25 SER B  306  GLU B  312  1                                   7    
HELIX   26  26 TYR B  329  PHE B  333  5                                   5    
SHEET    1   A 2 GLU A  19  CYS A  21  0                                        
SHEET    2   A 2 CYS A  27  SER A  29 -1  O  PHE A  28   N  VAL A  20           
SHEET    1   B10 ASN A  63  ILE A  70  0                                        
SHEET    2   B10 ARG A  55  THR A  60 -1  N  LEU A  58   O  GLN A  68           
SHEET    3   B10 VAL A 118  ASP A 124 -1  O  CYS A 120   N  TYR A  59           
SHEET    4   B10 LYS A  88  ILE A  93  1  N  ARG A  90   O  ILE A 121           
SHEET    5   B10 VAL A 165  HIS A 170  1  O  HIS A 166   N  PHE A  91           
SHEET    6   B10 ARG A 190  LEU A 194  1  O  LEU A 194   N  GLY A 169           
SHEET    7   B10 VAL A 218  ILE A 221  1  O  ILE A 221   N  GLY A 193           
SHEET    8   B10 LEU A 243  PRO A 247  1  O  PHE A 245   N  VAL A 220           
SHEET    9   B10 GLN A 342  LEU A 346  1  O  PHE A 344   N  PHE A 246           
SHEET   10   B10 TYR A 302  PRO A 303 -1  N  TYR A 302   O  PHE A 345           
SHEET    1   C 2 SER A 225  SER A 226  0                                        
SHEET    2   C 2 GLY A 235  MET A 236  1  O  GLY A 235   N  SER A 226           
SHEET    1   D 8 ASN A 385  LEU A 396  0                                        
SHEET    2   D 8 VAL A 371  TYR A 380 -1  N  LEU A 379   O  SER A 386           
SHEET    3   D 8 LYS A 417  ASN A 423 -1  O  LEU A 421   N  ARG A 376           
SHEET    4   D 8 GLN A 464  PRO A 468 -1  O  GLN A 464   N  PHE A 420           
SHEET    5   D 8 GLU A 449  CYS A 453 -1  N  CYS A 453   O  TYR A 467           
SHEET    6   D 8 LEU A 434  SER A 443 -1  N  VAL A 441   O  TYR A 450           
SHEET    7   D 8 TRP A 357  GLY A 367 -1  N  SER A 362   O  THR A 440           
SHEET    8   D 8 SER A 401  VAL A 408 -1  O  VAL A 408   N  TRP A 357           
SHEET    1   E 2 GLU B  19  CYS B  21  0                                        
SHEET    2   E 2 CYS B  27  SER B  29 -1  O  PHE B  28   N  VAL B  20           
SHEET    1   F10 GLN B  68  ILE B  70  0                                        
SHEET    2   F10 ARG B  55  TYR B  59 -1  N  LEU B  58   O  GLN B  68           
SHEET    3   F10 VAL B 118  ASP B 124 -1  O  CYS B 120   N  TYR B  59           
SHEET    4   F10 LYS B  88  ILE B  93  1  N  ARG B  90   O  ILE B 121           
SHEET    5   F10 VAL B 165  HIS B 170  1  O  HIS B 166   N  PHE B  91           
SHEET    6   F10 ARG B 190  LEU B 194  1  O  LEU B 194   N  GLY B 169           
SHEET    7   F10 PHE B 217  ILE B 221  1  O  PHE B 217   N  ILE B 191           
SHEET    8   F10 LEU B 243  PRO B 247  1  O  LEU B 243   N  VAL B 220           
SHEET    9   F10 GLN B 342  LEU B 346  1  O  GLN B 342   N  ASP B 244           
SHEET   10   F10 TYR B 302  PRO B 303 -1  N  TYR B 302   O  PHE B 345           
SHEET    1   G 2 SER B 225  SER B 226  0                                        
SHEET    2   G 2 GLY B 235  MET B 236  1  O  GLY B 235   N  SER B 226           
SHEET    1   H 8 TYR B 389  LEU B 396  0                                        
SHEET    2   H 8 VAL B 371  TYR B 380 -1  N  ILE B 377   O  TYR B 389           
SHEET    3   H 8 LYS B 417  ASN B 423 -1  O  LEU B 421   N  ARG B 376           
SHEET    4   H 8 GLN B 464  PRO B 468 -1  O  GLN B 464   N  PHE B 420           
SHEET    5   H 8 GLU B 449  CYS B 453 -1  N  CYS B 453   O  TYR B 467           
SHEET    6   H 8 LEU B 434  SER B 443 -1  N  VAL B 441   O  TYR B 450           
SHEET    7   H 8 TRP B 357  GLY B 367 -1  N  LYS B 360   O  GLN B 442           
SHEET    8   H 8 SER B 401  VAL B 408 -1  O  HIS B 402   N  VAL B 363           
SSBOND   1 CYS A   21    CYS A   27                          1555   1555  2.06  
SSBOND   2 CYS A  109    CYS A  120                          1555   1555  2.04  
SSBOND   3 CYS A  256    CYS A  280                          1555   1555  2.05  
SSBOND   4 CYS A  304    CYS A  315                          1555   1555  2.05  
SSBOND   5 CYS A  318    CYS A  323                          1555   1555  2.02  
SSBOND   6 CYS A  453    CYS A  469                          1555   1555  2.04  
SSBOND   7 CYS B   21    CYS B   27                          1555   1555  2.05  
SSBOND   8 CYS B  109    CYS B  120                          1555   1555  2.05  
SSBOND   9 CYS B  256    CYS B  280                          1555   1555  2.06  
SSBOND  10 CYS B  304    CYS B  315                          1555   1555  2.05  
SSBOND  11 CYS B  318    CYS B  323                          1555   1555  2.04  
SSBOND  12 CYS B  453    CYS B  469                          1555   1555  2.05  
LINK         C1  NAG A 500                 ND2 ASN A 353     1555   1555  1.45  
LINK         C1  NAG B 500                 ND2 ASN B 353     1555   1555  1.46  
LINK         O4  NAG A 500                 C1  NAG A 501     1555   1555  1.45  
LINK         O4  NAG A 501                 C1  MAN A 502     1555   1555  1.45  
LINK         O6  MAN A 502                 C1  MAN A 503     1555   1555  1.44  
LINK         O3  MAN A 502                 C1  MAN A 504     1555   1555  1.45  
LINK         O4  NAG B 500                 C1  NAG B 501     1555   1555  1.45  
LINK         O4  NAG B 501                 C1  MAN B 502     1555   1555  1.46  
LINK         O6  MAN B 502                 C1  MAN B 503     1555   1555  1.45  
LINK         O3  MAN B 502                 C1  MAN B 504     1555   1555  1.45  
LINK        CA    CA A 600                 OD1 ASP A 214     1555   1555  2.68  
LINK        CA    CA A 600                 O   ARG A 209     1555   1555  2.39  
LINK        CA    CA A 600                 O   GLU A 206     1555   1555  2.45  
LINK        CA    CA A 600                 OD2 ASP A 214     1555   1555  2.70  
LINK        CA    CA A 600                 O   HOH A 617     1555   1555  2.75  
LINK        CA    CA A 600                 OD2 ASP A 211     1555   1555  2.34  
LINK        CA    CA B 600                 O   ARG B 209     1555   1555  2.39  
LINK        CA    CA B 600                 OD2 ASP B 211     1555   1555  2.35  
LINK        CA    CA B 600                 OD1 ASP B 214     1555   1555  2.65  
LINK        CA    CA B 600                 OD2 ASP B 214     1555   1555  2.82  
LINK        CA    CA B 600                 O   GLU B 206     1555   1555  2.25  
CISPEP   1 LYS A   32    PRO A   33          0         2.63                     
CISPEP   2 VAL A  229    PRO A  230          0        -1.08                     
CISPEP   3 PHE A  316    PRO A  317          0        -5.22                     
CISPEP   4 LYS B   32    PRO B   33          0         9.53                     
CISPEP   5 VAL B  229    PRO B  230          0         0.43                     
CISPEP   6 PHE B  316    PRO B  317          0        -5.25                     
SITE     1 AC1  5 ASN A 353  THR A 355  PHE A 410  NAG A 501                    
SITE     2 AC1  5 HOH A 624                                                     
SITE     1 AC2  6 GLU A 384  ASN A 385  ASP A 409  PHE A 410                    
SITE     2 AC2  6 NAG A 500  MAN A 502                                          
SITE     1 AC3  4 ASN A 385  NAG A 501  MAN A 503  MAN A 504                    
SITE     1 AC4  1 MAN A 502                                                     
SITE     1 AC5  2 ASN A 385  MAN A 502                                          
SITE     1 AC6  5 ASN B 295  ASN B 353  THR B 355  ASP B 409                    
SITE     2 AC6  5 NAG B 501                                                     
SITE     1 AC7  4 ASP B 409  NAG B 500  MAN B 502  HOH B 614                    
SITE     1 AC8  5 ASN B 385  NAG B 501  MAN B 503  MAN B 504                    
SITE     2 AC8  5 HOH B 630                                                     
SITE     1 AC9  2 MAN B 502  HOH B 615                                          
SITE     1 BC1  3 ASN B 383  ASN B 385  MAN B 502                               
SITE     1 BC2  5 GLU A 206  ARG A 209  ASP A 211  ASP A 214                    
SITE     2 BC2  5 HOH A 617                                                     
SITE     1 BC3  4 GLU B 206  ARG B 209  ASP B 211  ASP B 214                    
SITE     1 BC4  1 ASN A  66                                                     
SITE     1 BC5  1 GLY B 255                                                     
SITE     1 BC6  2 LYS A  99  ARG B 126                                          
SITE     1 BC7  2 PRO B  64  ASN B  66                                          
CRYST1  216.922  216.922  123.618  90.00  90.00  90.00 I 41 2 2     32          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004610  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004610  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008089        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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